title: Isolation, crystallization and preliminary X-ray diffraction analysis of L-amino-acid oxidase from Vipera ammodytes ammodytes venom.
abstract: L-Amino-acid oxidase from the venom of Vipera ammodytes ammodytes, the most venomous snake in Europe, was isolated and crystallized using the sitting-drop vapour-diffusion method. The solution conditions under which the protein sample was monodisperse were optimized using dynamic light scattering prior to crystallization. The crystals belonged to space group C2, with unit-cell parameters a = 198.37, b = 96.38, c = 109.11 A, beta = 92.56 degrees . Initial diffraction data were collected to 2.6 A resolution. The calculated Matthews coefficient is approximately 2.6 A(3) Da(-1) assuming the presence of four molecules in the asymmetric unit.
authors.affiliation: Institute of Biochemistry and Molecular Biology, University of Hamburg, c/o DESY, Gebäude 22a, Notkestrasse 85, 22603 Hamburg, Germany.
authors.forename: Dessislava
authors.initials: D
authors.lastname: Georgieva
authors.forename: Anna
authors.initials: A
authors.lastname: Kardas
authors.forename: Friedrich
authors.initials: F
authors.lastname: Buck
authors.forename: Markus
authors.initials: M
authors.lastname: Perbandt
authors.forename: Christian
authors.initials: C
authors.lastname: Betzel
mesh_terms: D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D050830:L-Amino Acid Oxidase / Q000737:chemistry* / Q000302:isolation & purification; D012996:Solutions; D014757:Viper Venoms / Q000737:chemistry* / Q000302:isolation & purification; D017819:Viperidae; D014961:X-Ray Diffraction / Q000379:methods
chemical_list: D012996:Solutions; D014757:Viper Venoms; D050830:L-Amino Acid Oxidase